Identification and characterization of GSTT3, a third murine Theta class glutathione transferase

Marjorie Coggan, Jack U. Flanagan, Michael W. Parker, Vanicha Vichai, William R. Pearson, Philip G. Board*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    24 Citations (Scopus)

    Abstract

    A novel Theta class glutathione transferase (GST) isoenzyme from mouse termed mGSTT3 has been identified by analysis of the expressed sequence tag database. The gene encoding mGSTT3 is clustered with the mGSTT1 and mGSTT2 genes on chromosome 10 and has an exon/intron structure that is similar to that of the other Theta class genes. mGSTT3 is expressed strongly in the liver and to a decreasing extent in the kidney and testis. Recombinant mGSTT3-3 expressed in Escherichia coli had a substrate-specificity profile that differed significantly from that of GSTT1-1 and GSTT2-2 isoenzymes. A molecular model of mGSTT3 suggested that, in comparison with GSTT2, a decrease in volume of the hydrophobic substrate-binding site and the loss of the sulphate-binding pocket prevents its use of the GSTT2 substrate 1-menaphthyl sulphate.

    Original languageEnglish
    Pages (from-to)323-332
    Number of pages10
    JournalBiochemical Journal
    Volume366
    Issue number1
    DOIs
    Publication statusPublished - 15 Aug 2002

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